Esterolytic, elastase-like activity of purified alkaline proteinase from Aspergillus sojae

Abstract

1. 1. The ester bond of acetyl- l-alanyl- l-alanyl- l-alanine methyl ester is hydrolysed by the alkaline proteinase from Aspergillus sojae in the pH range of 7–10. The K m and k cat values at 30°, pH 8.5, are 21.6 mM and 2800 sec −1. 2. 2. The alkaline proteinase possesses weak esterolytic activity on α-N- benzoyl- l-arginine ethyl ester and N- acetyl- l-tyrosine ethyl ester. This activity is not inhibited by natural and synthetic inhibitors of trypsin and chymotrypsin. 3. 3. Alkaline proteinase does not hydrolyse elastin since its slightly acidic nature prevents its adsorbtion on insoluble elastin.